Linked Life Data

2015897

Source:http://linkedlifedata.com/resource/pubmed/id/2015897

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1991-5-21
pubmed:abstractText
The solution conformation of a 21-residue vasoconstrictor peptide endothelin-1 (ET-1) in water-ethylene glycol has been determined by two-dimensional 1H-NMR spectroscopy and constrained molecular dynamics simulations. The N-terminus (residues 1-4) appears to undergo conformational averaging and no single structure consistent with the NMR constraints could be found for this region. Residues 5-8 form a turn, and residues 9-16 exist in a helical conformation. A flexible 'hinge' between residues 8-9 allows various orientations of the turn relative to the helix. Another 'hinge' at residue 17 connects the extended C-terminus to the bicyclic core region (residues 1-15). Residues important for binding and biological activity form a contiguous surface on one side of the helix, with the two disulfides extending from the other side of the helix.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
281
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
212-8
pubmed:dateRevised
2001-3-23
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Conformation of endothelin in aqueous ethylene glycol determined by 1H-NMR and molecular dynamics simulations.
pubmed:affiliation
Department of Macromolecular Modeling, Bristol-Myers Squibb Research Institute, Princeton, NJ 08543-4000.
pubmed:publicationType
Journal Article